ID   LEU1_BUCUN              Reviewed;         502 AA.
AC   Q9EVI8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 67.
DE   RecName: Full=2-isopropylmalate synthase;
DE            EC=2.3.3.13;
DE   AltName: Full=Alpha-IPM synthase;
DE   AltName: Full=Alpha-isopropylmalate synthase;
DE   Flags: Fragment;
GN   Name=leuA;
OS   Buchnera aphidicola subsp. Uroleucon sonchi.
OG   Plasmid pLeu (pBAp1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11133977; DOI=10.1128/jb.183.2.785-790.2001;
RA   Wernegreen J.J., Moran N.A.;
RT   "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT   (Buchnera).";
RL   J. Bacteriol. 183:785-790(2001).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000305}.
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DR   EMBL; AF197448; AAG31377.1; -; Genomic_DNA.
DR   UniPathway; UPA00048; UER00070.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 1.
DR   HAMAP; MF_01025; LeuA_type1; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR005671; LeuA_bact_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00973; leuA_bact; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Leucine biosynthesis; Plasmid; Transferase.
FT   CHAIN           <1..502
FT                   /note="2-isopropylmalate synthase"
FT                   /id="PRO_0000140345"
FT   DOMAIN          <1..254
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   NON_TER         1
SQ   SEQUENCE   502 AA;  55842 MW;  18DD7CFB4245F4F3 CRC64;
     DGEQALQASL SVKEKLQIAL CLEKAGVDIM EVGFPISSPG DFKSVQTISQ NIKNSRICSL
     ARCIEKDIDT AGEAMSHCDF FRIHVFLATS TLHMESKLRK NFDEIIDMAI FSVKRALRYT
     DDVEFSCEDA SRTTMDNLCR IVEKLISCGV KTINIPDTVG YTIPNELSLI IKNLFERVPN
     IHKSTISVHC HNDLGMAVGN SISAIQAGAR QIEGTINGIG ERAGNTALEE VIMAIKVRED
     ILGLSTNINH KEIYRTSQVI SRICNMPIPS NKAIVGSNAF SHSSGIHQDG VLKNRENYEI
     MDPSSIGLKK VKLNLTSRSG RAAVKYYMNE MGYKDSDYNI DELYVDFLKL ADKKGQVFDY
     DLEALAFINK KQDELEHFCL KFFSVQSISN NLSTASVTLL CGDKIYTESS TTSNGPVXAI
     YQALNRITHF PIILQKFQLI AKGQGKDALG QVDILVKYKK RQFHGVGLAT DIIESSAQAM
     INVLNNIWKV KQVNKNLKNL KK